1
40
2
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
URL Address
<a href="http://doi.org/10.1167/iovs.15-17885" target="_blank" rel="noreferrer noopener">http://doi.org/10.1167/iovs.15-17885</a>
Rights
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
Pages
8215-8227
Issue
13
Volume
56
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Dublin Core
The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
A name given to the resource
Decreased Energy Capacity And Increased Autophagic Activity In Optic Nerve Axons With Defective Anterograde Transport
Publisher
An entity responsible for making the resource available
Investigative Ophthalmology & Visual Science
Date
A point or period of time associated with an event in the lifecycle of the resource
2015
2015-12
Subject
The topic of the resource
anterograde transport; autophagy; cholera; cholera-toxin; degeneration; dying back process; endoplasmic-reticulum; glaucoma; microscopy; Mitochondria; mitophagy; mouse model; Ophthalmology; optic neuropathy; stress; toxin-B
Creator
An entity primarily responsible for making the resource
Kleesattel D; Crish S D; Inman D M
Description
An account of the resource
PURPOSE. Autophagy is a critical process, compromised in neurodegenerative disease, by which terminally differentiated cells like neurons manage cytoskeletal and organelle turnover. How autophagy relates to associated neurodegenerative pathologies remain unclear. We examined autophagy in optic neuropathy by investigating cytoskeletal degradation, mitochondria, and autophagic vesicles in the DBA2/J mouse model of glaucoma exhibiting differing levels of axon transport functionality. METHODS. DBA/2J and DBA/2J(wt-gpnmb) control mice 11 to 14 months of age were injected with cholera toxin-B (CTB) to assay anterograde axonal transport. Axonal mitochondria and autophagic vesicles were analyzed with respect to transport integrity in proximal and distal optic nerve using serial block face scanning electron microscopy (3D EM). RESULTS. Several indices varied significantly between the DBA/2J and DBA/2Jwt-gpnmb mice, including mitochondrial volume, average number of autophagic vesicles per axon, and mitochondrial cristae. However, there were no differences in mitochondrial cristae for axons with functional versus dysfunctional CTB transport, suggesting that mitochondrial dysfunction precedes overt transport blockade. Anterograde transport failure was accompanied by a dissociation of the relationship between mitochondrial and axon volumes. Autophagic vesicle profiles were significantly increased in optic nerve with transport deficit, consistent with greater autophagic activity. Mitochondria within autophagosomes, indicative of mitophagy, were observed in both proximal and distal axons. CONCLUSIONS. Loss of anterograde transport in DBA/2J optic nerve is concomitant with diminished mitochondrial volume, increased cytoskeletal breakdown and autophagic activity, and accumulation of autophagic profiles, including signs of mitophagy, in proximal optic nerve. Axons with transport deficit are metabolically underserved, though not necessarily from mitophagy.
Identifier
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<a href="http://doi.org/10.1167/iovs.15-17885" target="_blank" rel="noreferrer noopener">10.1167/iovs.15-17885</a>
Format
The file format, physical medium, or dimensions of the resource
Journal Article or Conference Abstract Publication
2015
anterograde transport
Autophagy
Cholera
cholera-toxin
Crish S D
degeneration
Department of Pharmaceutical Sciences
dying back process
endoplasmic-reticulum
Glaucoma
Inman D M
Investigative ophthalmology & visual science
Journal Article or Conference Abstract Publication
Kleesattel D
Microscopy
Mitochondria
mitophagy
Mouse model
NEOMED College of Pharmacy
Ophthalmology
optic neuropathy
Stress
toxin-B
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
URL Address
<a href="http://doi.org/10.1002/1098-2299(20000901)51:1%3C7::aid-ddr2%3E3.3.co;2-n" target="_blank" rel="noreferrer noopener">http://doi.org/10.1002/1098-2299(20000901)51:1%3C7::aid-ddr2%3E3.3.co;2-n</a>
Rights
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
Pages
7-19
Issue
1
Volume
51
Search for Full-text
Locate full-text within NEOMED Library's e-journal collections
<p>Users with a NEOMED Library login can search for full-text journal articles at the following url: <a href="https://libraryguides.neomed.edu/home">https://libraryguides.neomed.edu/home</a></p>
Dublin Core
The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
A name given to the resource
Purification and recognition of recombinant mouse P2X(1) receptors expressed in a baculovirus system
Publisher
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Drug Development Research
Date
A point or period of time associated with an event in the lifecycle of the resource
2000
2000-09
Subject
The topic of the resource
Pharmacology & Pharmacy; protein; binding; gated ion channels; agonist; cation channels; activation; extracellular; site; Ion channels; endoplasmic-reticulum; affinity chromatography; ATP; nadph-p450 oxidoreductase; nucleotides; p-2x receptors; polyacrylamide-gel electrophoresis; structural motif
Creator
An entity primarily responsible for making the resource
Chen L P; Hardwick J P; McPhie P; Sitkovsky M V; Jacobson K A
Description
An account of the resource
The hexahistidine-tagged mouse P2X(1) receptor (H-mP2X(1)R), an ATP-gated ion channel receptor, was expressed in a baculovirus system using the pAcHLT-B transfer vector containing a hexahistidine tag. Both widely used denaturing (8M urea) acid nondenaturing (such as 1% Triton X-100) solubilization conditions were compared, resulting in about 30% of the P2X(1) receptors being solubilized (S1). However, at pH 13 most of the n-mP2X(1)R from the initially insoluble pellet fraction was solubilized (S2) and remained in the soluble fraction (S3) after dialyzing against a nondenaturing buffer. H-mP2X(1)Rs were purified sequentially through cobalt and ATP affinity columns. Receptors purified from S3 had higher purity than those from S1 (i.e., similar to 90% vs. similar to 75%). Circular dichroism spectra indicated identical protein secondary structures of the receptors from both sources. Autoradiographic data showed that the purified receptors from S3 had higher affinity for 8-azido-ATP-gamma-P-32 than the receptors from S1. The binding of 8-azido-ATP-gamma-P-32 to H-mP2X(1)R was inhibited by ATP-gamma -S, alpha,beta -me-ATP, and PPADS, but not by a nucleoside analog (N-6-methyl-2'-deoxy-adenosine). In the presence of 2 mM Ca2+ or Mg2+ the binding was increased, but not when using a partially purified receptor fraction, in which unidentified proteins bound 8-azido ATP-gamma-P-32 or were phosphorylated at 4 degreesC in the presence of 2 mM Mg2+. These data suggest that the decrease in potency of ATP in the presence of Ca2+ and Mg2+, as observed in functional studies, is not due to a direct effect of the cations on the binding of ATP to the receptor. Both cyanogen bromide and hydroxylamine cleavage further confirmed the peptide structure of the purified H-mP2X1R. Autoradiographic analysis of the cleavage products showed that 8-azido-ATP-gamma-P-32 was crosslinked to the carboxyl side of the extracellular domain of the receptor. Drug Dev. Res. 51:7-19, 2000. Published 2000 Wiley-Liss, Inc.dagger
Identifier
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<a href="http://doi.org/10.1002/1098-2299(20000901)51:1%3C7::aid-ddr2%3E3.3.co;2-n" target="_blank" rel="noreferrer noopener">10.1002/1098-2299(20000901)51:1%3C7::aid-ddr2%3E3.3.co;2-n</a>
Format
The file format, physical medium, or dimensions of the resource
Journal Article or Conference Abstract Publication
2000
activation
affinity chromatography
agonist
ATP
Binding
cation channels
Chen L P
Drug Development Research
endoplasmic-reticulum
extracellular
gated ion channels
Hardwick J P
Ion Channels
Jacobson K A
Journal Article or Conference Abstract Publication
McPhie P
nadph-p450 oxidoreductase
nucleotides
p-2x receptors
Pharmacology & Pharmacy
polyacrylamide-gel electrophoresis
Protein
site
Sitkovsky M V
structural motif